Reviewed, UniProtKB/Swiss-Prot Q6BUP9 (ARGD_DEBHA)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase, mitochondrial
      Short name=ACOAT
    EC=2.6.1.11

Gene names

Name:	ARG8
Ordered Locus Names:	DEHA2C09042g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 466		Acetylornithine aminotransferase, mitochondrial		PRO_0000002078
Amino acid modifications
	Modified residue	308	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BUP9-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 7AEE29F6C69BFAC7	FASTA	466	50,653
	10 20 30 40 50 60 MLRNIPRSLR KDGGKRIPGL ISRVANQFST TSSLLNKKSI PDAPEDSHTG QYINTITKPF 70 80 90 100 110 120 TVTTYARPNV VMTHGKGSYL YDLENRQYLD FSAGIAVTCL GHSHSKITEI ISDQAATLMH 130 140 150 160 170 180 CSNLYHNLYA GELANKLVTN TINSGGMKEA QRVFLCNSGT EANEAALKFA RKYGKSFSDD 190 200 210 220 230 240 KYEMITFKNS FHGRTMGALS VTPNEKYQKP FAPLVPGVKI AEPNDISSVE KLISKEKTCA 250 260 270 280 290 300 VIIEPIQGEG GVNAIDAEFL VSLKKLCVDN EVVLIYDEIQ CGLGRSGKLW AHCNLPEEAH 310 320 330 340 350 360 PDILTMAKAL GNGFPIGAVM VSDKIEKVLK VGDHGTTYGG NPLGSKIGSY VVDQVSDKEF 370 380 390 400 410 420 LLEVEEKSEK FTKGLSKIAN KHPDHIGEVK GKGLLLGLQL KGNLDVGDVV AKCRENGLLV 430 440 450 460 ISAGMNVLRI VPALNIPNEA IEEGLDVLDK CIDELSKDPK SSFSQS

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382135 Genomic DNA. Translation: CAG86141.1.
RefSeq	XP_458070.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BUP9.
Genome annotation databases
GeneID	2900662.
GenomeReviews	Gene locus DEHA2C09042g in contig CR382135_GR.
KEGG	dha:DEHA0C09955g.
Phylogenomic databases
HOGENOM	Q6BUP9.
OMA	TTYARPN.
Enzyme and pathway databases
BRENDA	2.6.1.11. 74267.
Family and domain databases
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00707. argD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_DEBHA

Accession

Primary (citable) accession number: Q6BUP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)